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Structure of reduced cytochrome C6 from synechococcus sp. pcc 7002

Analyse Structure of reduced cytochrome C6 from synechococcus sp. pcc 7002 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3DR0
Type
protein
Length
279 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Cytochrome C6
UniProt
O30881
Ligands
HEM, SO4
Pockets
3 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 56% helix, 4% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, CCytochrome C6protein9356% helix, 4% strandO30881

Ligands and binding sites

  • HEM · Protoporphyrin IX containing Fe · ligand · 3 copies · chains A, B, C
  • SO4 · Sulfate ion · ion · 2 copies · chains B, C

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11910.710.8831HEM
23040.710.8444HEM
32000.700.8730HEM

Interfaces

2 interfaces between chains.

  • B–C · 381 Ų buried · 7 hydrogen bonds · protein-protein
  • A–B · 139 Ų buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 cofactor (heme attachment).

Compared structures

  • 3DR0 · Structure of reduced cytochrome c6 from Synechococcus sp. PCC 7002 · the same entry in another collection · chain B against B, TM-score 1.00
  • O30881 · AlphaFold monomer V2.0 prediction for cytochrome C6 (O30881) · a predicted model of the same protein · chain A against A, TM-score 0.99

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